1990
[21] Reversed-phase high-performance liquid chromatography for fractionation of enzymatic digests and chemical cleavage products of proteins
Stone K, Elliott J, Peterson G, McMurray W, Williams K. [21] Reversed-phase high-performance liquid chromatography for fractionation of enzymatic digests and chemical cleavage products of proteins. Methods In Enzymology 1990, 193: 389-412. PMID: 2074828, DOI: 10.1016/0076-6879(90)93429-o.Peer-Reviewed Original ResearchConceptsHigh-performance liquid chromatographyReversed-phase high-performance liquid chromatographyReversed phase high performance liquid chromatographyLiquid chromatographyEnzymatic digestsHigh peak capacityMass spectrometric approachProtein chemistsSpectrometric approachMass spectrometryPeak capacityComplex mixturesMolecular weightChemical cleavageGradient timeCleavage productsChromatographyTryptic peptidesPeptidesDigestsChemistsSpectrometryFractionationProductsPrimary structure
1987
Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking.
Pandey V, Williams K, Stone K, Modak M. Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking. Biochemistry 1987, 26: 7744-8. PMID: 3322406, DOI: 10.1021/bi00398a031.Peer-Reviewed Original ResearchConceptsCross-linking reactionReversed-phase high-performance liquid chromatographyHigh-performance liquid chromatographyCross-linking sitesEscherichia coli DNA polymerase IPeptide lossKlenow fragmentChelate formLiquid chromatographyAmino acid analysisE. coli DNA Pol ISmall peptidesTryptic digestionSubstrate deoxynucleoside triphosphateHistidine residuesTryptic peptidesAmino acidsSingle peptideOptimal conditionsPeptide mappingDNA Pol IStaphylococcus aureus V8 protease digestionDNA polymerase IAcceptor sitesPeptides